Abstract
Recent reports have provided the first insights into the mechanisms of the extensive post-translational modifications involved in the biosynthesis of the lantibiotics, a class of peptide antimicrobial agents. These modifications involve dehydration of several serine and threonine residues followed by intramolecular conjugate additions of cysteines, resulting in extensively cross-linked polycyclic structures. Both in vivo and in vitro studies indicate low substrate specificity of the modification machinery, which has been explored for re-engineering of the structures of a number of members. In addition to these developments in understanding their biosynthesis, studies on the mode of action of several lantibiotics have shown a unique mechanism of binding to lipid II, an intermediate in cell wall biosynthesis.
Original language | English (US) |
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Pages (from-to) | 498-507 |
Number of pages | 10 |
Journal | Current Opinion in Chemical Biology |
Volume | 8 |
Issue number | 5 |
DOIs | |
State | Published - Oct 2004 |
Keywords
- (Z)-2,3-dehydrobutyrine
- 2,3-dehydroalanine
- Dha
- Dhb
- Lan
- MeLan
- lanthionine
- methyllanthionine
ASJC Scopus subject areas
- Analytical Chemistry
- Biochemistry